[HTML][HTML] Fucose-binding lectin from opportunistic pathogen Burkholderia ambifaria binds to both plant and human oligosaccharidic epitopes

A Audfray, J Claudinon, S Abounit… - Journal of Biological …, 2012 - ASBMB
Burkholderia ambifaria is generally associated with the rhizosphere of plants where it has
biocontrol effects on other microorganisms. It is also a member of the Burkholderia cepacia …

New natural intergenotypic (2/5) recombinant of hepatitis C virus

F Legrand-Abravanel, J Claudinon, F Nicot… - Journal of …, 2007 - Am Soc Microbiol
A 9.2-kb sequence from a hepatitis C virus (HCV) strain found in southwest France was
compared to sequences from reference strains in HCV sequence databases. We found a …

[HTML][HTML] Plasma membrane reorganization: A glycolipid gateway for microbes

S Aigal, J Claudinon, W Römer - … et Biophysica Acta (BBA)-Molecular Cell …, 2015 - Elsevier
Ligand–receptor interactions, which represent the core for cell signaling and internalization
processes are largely affected by the spatial configuration of host cell receptors. There is a …

Membrane deformation by neolectins with engineered glycolipid binding sites

J Arnaud, K Tröndle, J Claudinon, A Audfray… - Angewandte …, 2014 - Wiley Online Library
Lectins are glycan‐binding proteins that are involved in the recognition of glycoconjugates
at the cell surface. When binding to glycolipids, multivalent lectins can affect their distribution …

Dynamic cooperative glycan assembly blocks the binding of bacterial lectins to epithelial cells

…, É Gillon, S Zheng, J Claudinon… - Angewandte Chemie …, 2017 - Wiley Online Library
Pathogens frequently rely on lectins for adhesion and cellular entry into the host. Since these
interactions typically result from multimeric binding of lectins to cell‐surface glycans, novel …

[HTML][HTML] Palmitoylation of interferon-α (IFN-α) receptor subunit IFNAR1 is required for the activation of Stat1 and Stat2 by IFN-α

J Claudinon, P Gonnord, E Beslard, M Marchetti… - Journal of biological …, 2009 - ASBMB
Type I interferons (IFNs) bind IFNAR receptors and activate Jak kinases and Stat transcription
factors to stimulate the transcription of genes downstream from IFN-stimulated response …

Reduction of lectin valency drastically changes glycolipid dynamics in membranes but not surface avidity

J Arnaud, J Claudinon, K Tröndle… - ACS chemical …, 2013 - ACS Publications
Multivalency is proposed to play a role in the strong avidity of lectins for glycosylated cell
surfaces and also in their ability to affect membrane dynamics by clustering glycosphingolipids. …

Carbohydrate-dependent B cell activation by fucose-binding bacterial lectins

…, P Müller, A Imberty, R Thuenauer, J Claudinon… - Science …, 2019 - science.org
Bacterial lectins are typically multivalent and bind noncovalently to specific carbohydrates
on host tissues to facilitate bacterial adhesion. Here, we analyzed the effects of two fucose-…

Interfering with interferon receptor sorting and trafficking: impact on signaling

J Claudinon, MN Monier, C Lamaze - Biochimie, 2007 - Elsevier
Interferons (IFNs) and their receptors (IFN-Rs) play fundamental roles in a multitude of
biological functions. Many articles and reviews emphasize that the JAK/STAT machinery is …

Pseudomonas aeruginosa lectin LecB impairs keratinocyte fitness by abrogating growth factor signalling

…, A Nyström, F Reggiori, J Claudinon… - Life science …, 2019 - life-science-alliance.org
Lectins are glycan-binding proteins with no catalytic activity and ubiquitously expressed in
nature. Numerous bacteria use lectins to efficiently bind to epithelia, thus facilitating tissue …